Calmodulin interacts with angiotensin-converting enzyme-2 (ACE2) and inhibits shedding of its ectodomain.
Angiotensin-converting enzyme-2 (ACE2) is a regulatory protein of the renin-angiotensin system (RAS) and a receptor for the causative agent of severe-acute respiratory syndrome (SARS), the SARS-coronavirus. We have previously shown that ACE2 can be shed from the cell surface in response to phorbol esters by a process involving TNF-alpha converting ... enzyme (TACE; ADAM17). In this study, we demonstrate that inhibitors of calmodulin also stimulate shedding of the ACE2 ectodomain, a process at least partially mediated by a metalloproteinase. We also show that calmodulin associates with ACE2 and that this interaction is decreased by calmodulin inhibitors.
Mesh Terms:
Amino Acid Sequence, Calmodulin, Cell Line, Dipeptides, Humans, Immunoprecipitation, Molecular Sequence Data, Peptidyl-Dipeptidase A, Protease Inhibitors, Protein Binding, Sequence Homology, Amino Acid
Amino Acid Sequence, Calmodulin, Cell Line, Dipeptides, Humans, Immunoprecipitation, Molecular Sequence Data, Peptidyl-Dipeptidase A, Protease Inhibitors, Protein Binding, Sequence Homology, Amino Acid
FEBS Lett.
Date: Jan. 23, 2008
PubMed ID: 18070603
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